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Solution conformation of a peptide corresponding to the principal neutralizing determinant of HIV-1IIIB: a two-dimensional NMR study.
Zvi A, Hiller R, Anglister J. Zvi A, et al. Biochemistry. 1992 Aug 4;31(30):6972-9. doi: 10.1021/bi00145a015. Biochemistry. 1992. PMID: 1637831
A helical conformation was found to be stabilized by the addition of TFE. A transient turn was observed also in the GPGR sequence, both in water and in aqueous TFE solutions. While no nascent helix conformations could be observed in the N-terminal part of RP135 in w
A helical conformation was found to be stabilized by the addition of TFE. A transient turn was observed also in the GPGR seque
Expression, purification, and isotope labeling of the Fv of the human HIV-1 neutralizing antibody 447-52D for NMR studies.
Kessler N, Zvi A, Ji M, Sharon M, Rosen O, Levy R, Gorny M, Zolla-Pazner S, Anglister J. Kessler N, et al. Protein Expr Purif. 2003 Jun;29(2):291-303. doi: 10.1016/s1046-5928(03)00047-0. Protein Expr Purif. 2003. PMID: 12767822
A pelB signal peptide was linked to the antibody genes to enable secretion of the expressed polypeptides into the periplasm. ...A set of oligonucleotides that prime the leader peptide genes of all potential antibody human antibodies were designed as backward primers
A pelB signal peptide was linked to the antibody genes to enable secretion of the expressed polypeptides into the periplasm. ...A
NMR structure of an anti-gp120 antibody complex with a V3 peptide reveals a surface important for co-receptor binding.
Tugarinov V, Zvi A, Levy R, Hayek Y, Matsushita S, Anglister J. Tugarinov V, et al. Structure. 2000 Apr 15;8(4):385-95. doi: 10.1016/s0969-2126(00)00119-2. Structure. 2000. PMID: 10801487
The bound peptide assumes a beta-hairpin conformation with a QRGPGR loop located at the very center of the binding pocket. The Fv and peptide surface areas buried upon binding are 601 A and 743 A(2), respectively, in the 0.5beta Fv-P1053 mean structure …
The bound peptide assumes a beta-hairpin conformation with a QRGPGR loop located at the very center of the binding pocket. The …
A model of a gp120 V3 peptide in complex with an HIV-neutralizing antibody based on NMR and mutant cycle-derived constraints.
Zvi A, Tugarinov V, Faiman GA, Horovitz A, Anglister J. Zvi A, et al. Eur J Biochem. 2000 Feb;267(3):767-79. doi: 10.1046/j.1432-1327.2000.01055.x. Eur J Biochem. 2000. PMID: 10651813
A deuterated V3 peptide and a Fab containing deuterated aromatic amino acids were used to assign these interactions to specific V3 residues and to the amino acid type and specific chain of the antibody by NOE difference spectroscopy. ...The peptide converges to a
A deuterated V3 peptide and a Fab containing deuterated aromatic amino acids were used to assign these interactions to specifi
A cis proline turn linking two beta-hairpin strands in the solution structure of an antibody-bound HIV-1IIIB V3 peptide.
Tugarinov V, Zvi A, Levy R, Anglister J. Tugarinov V, et al. Nat Struct Biol. 1999 Apr;6(4):331-5. doi: 10.1038/7567. Nat Struct Biol. 1999. PMID: 10201400
The refined solution structure of an 18-residue HIV-1IIIB V3 peptide in complex with the Fv fragment of an anti-gp120 antibody reveals an unexpected type VI beta-turn comprising residues RGPG at the center of a beta-hairpin. ...These differences could be due to a tw …
The refined solution structure of an 18-residue HIV-1IIIB V3 peptide in complex with the Fv fragment of an anti-gp120 antibody reveals an un …
Solid-state NMR evidence for an antibody-dependent conformation of the V3 loop of HIV-1 gp120.
Weliky DP, Bennett AE, Zvi A, Anglister J, Steinbach PJ, Tycko R. Weliky DP, et al. Nat Struct Biol. 1999 Feb;6(2):141-5. doi: 10.1038/5827. Nat Struct Biol. 1999. PMID: 10048925
Solid-state NMR measurements have been carried out on frozen solutions of the complex of a 24-residue peptide derived from the third variable (V3) loop of the HIV-1 envelope glycoprotein gp120 bound to the Fab fragment of an anti-gp120 antibody. ...These measurements are t …
Solid-state NMR measurements have been carried out on frozen solutions of the complex of a 24-residue peptide derived from the third …
Conformation of the principal neutralizing determinant of human immunodeficiency virus type 1 in complex with an anti-gp120 virus neutralizing antibody studied by two-dimensional nuclear magnetic resonance difference spectroscopy.
Zvi A, Feigelson DJ, Hayek Y, Anglister J. Zvi A, et al. Biochemistry. 1997 Jul 15;36(28):8619-27. doi: 10.1021/bi970520f. Biochemistry. 1997. PMID: 9214308
A total of 39 long-range (residues i - j >> 4), 14 short-range, and 69 intraresidue NOE interactions within the bound peptide have been assigned. Twelve structures without NOE constraint violations were obtained, having a 1.6 A rms deviation for the bac
A total of 39 long-range (residues i - j >> 4), 14 short-range, and 69 intraresidue NOE interactions within the bound peptide h
Two-dimensional NMR investigations of the interactions of antibodies with peptide antigens.
Anglister J, Scherf T, Zilber B, Levy R, Zvi A, Hiller R, Feigelson D. Anglister J, et al. FASEB J. 1993 Sep;7(12):1154-62. doi: 10.1096/fasebj.7.12.8375614. FASEB J. 1993. PMID: 8375614
Comparison of the interactions of three antibodies against a cholera toxin peptide (CTP3), which differ in their cross-reactivity with the toxin, yields information about the size and conformation of antigenic determinants recognized by antibodies, the structure of their c …
Comparison of the interactions of three antibodies against a cholera toxin peptide (CTP3), which differ in their cross-reactivity wit …
The principal neutralizing determinant of HIV-1 located in V3 of gp120 forms a 12-residue loop by internal hydrophobic interactions.
Zvi A, Kustanovich I, Hayek Y, Matsushita S, Anglister J. Zvi A, et al. FEBS Lett. 1995 Jul 17;368(2):267-70. doi: 10.1016/0014-5793(95)00669-z. FEBS Lett. 1995. PMID: 7543061
These measurements reveal hydrophobic interactions within the bound peptide between Ile-4, Ile-6 and Val-15 that create a 12-residue loop with these residues at the base and the conserved GPGR sequence at its top....
These measurements reveal hydrophobic interactions within the bound peptide between Ile-4, Ile-6 and Val-15 that create a 12-residue …
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